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Surface plasmon resonance sensing: from purified biomolecules to intact cells

Authors :
Wei Wang
Yu-wen Su
Source :
Analytical and Bioanalytical Chemistry. 410:3943-3951
Publication Year :
2018
Publisher :
Springer Science and Business Media LLC, 2018.

Abstract

Surface plasmon resonance (SPR) has become a well-recognized label-free technique for measuring the binding kinetics between biomolecules since the invention of the first SPR-based immunosensor in 1980s. The most popular and traditional format for SPR analysis is to monitor the real-time optical signals when a solution containing ligand molecules is flowing over a sensor substrate functionalized with purified receptor molecules. In recent years, rapid development of several kinds of SPR imaging techniques have allowed for mapping the dynamic distribution of local mass density within single living cells with high spatial and temporal resolutions and reliable sensitivity. Such capability immediately enabled one to investigate the interaction between important biomolecules and intact cells in a label-free, quantitative, and single cell manner, leading to an exciting new trend of cell-based SPR bioanalysis. In this Trend Article, we first describe the principle and technical features of two types of SPR imaging techniques based on prism and objective, respectively. Then we survey the intact cell-based applications in both fundamental cell biology and drug discovery. We conclude the article with comments and perspectives on the future developments. Graphical abstract Recent developments in surface plasmon resonance (SPR) imaging techniques allow for label-free mapping the mass-distribution within single living cells, leading to great expansions in biomolecular interactions studies from homogeneous substrates functionalized with purified biomolecules to heterogeneous substrates containing individual living cells.

Details

ISSN :
16182650 and 16182642
Volume :
410
Database :
OpenAIRE
Journal :
Analytical and Bioanalytical Chemistry
Accession number :
edsair.doi.dedup.....31d818918e5283a87ad882b719b82de1
Full Text :
https://doi.org/10.1007/s00216-018-1008-8